食品科学2025，Vol.46Issue(7)：43-50,8.DOI:10.7506/spkx1002-6630-20240520-174
肽Tyr-Pro-Ile-Trp(YPIW)对α-葡萄糖苷酶的抑制机理及其稳定性
Mechanism for the Inhibition of α-Glucosidase by Peptide Tyr-Pro-Ile-Trp(YPIW)and Its Stability
摘要
Abstract
In order to investigate the inhibitory effect of a novel bioactive peptide,Tyr-Pro-Ile-Trp(YPIW),on α-glucosidase,a variety of analytical methods including enzyme inhibition kinetics,ultraviolet(UV)absorption spectroscopy and Fourier transform infrared spectroscopy(FTIR)were employed to investigate the underlying inhibitory mechanism.Besides,the stability and cytotoxicity of YPIW were evaluated.The results indicated that YPIW exerted a significant inhibitory effect on α-glucosidase(half maximal inhibitory concentration(IC50)=1.03 mmol/L),which was comparable to that of acarbose(IC50=1.08 mmol/L).In the mixed competition mode,YPIW could reversibly inhibit the activity of α-glucosidase,and was more likely to bind with free α-glucosidase.The UV and FTIR showed that YPIW interacted with α-glucosidase,potentially altering the conformation of the enzyme,thereby reducing its catalytic activity.YPIW remained stable at low temperatures or in acidic environments,and had good tolerance to simulated gastrointestinal digestion.In addition,it had no obvious toxic effect on HepG2 cells in the concentration range of 0-1 mmol/L.This study provides a theoretical basis for the development of YPIW as a novel hypoglycemic peptide.关键词
α-葡萄糖苷酶抑制肽/抑制机理/光谱学/稳定性/细胞毒性Key words
α-glucosidase inhibitory peptide/inhibition mechanism/spectroscopy/stability/cytotoxicity分类
轻工业引用本文复制引用
陶强,李姣,曹皖雪,陈乃东..肽Tyr-Pro-Ile-Trp(YPIW)对α-葡萄糖苷酶的抑制机理及其稳定性[J].食品科学,2025,46(7):43-50,8.基金项目
安徽省中药质量评价与品质提升科研创新团队项目(2022AH010090) （2022AH010090）
安徽省高校协同创新中心项目(GXXT-2022-079) （GXXT-2022-079）
皖西学院高层次人才启动项目(WGKQ2022024) （WGKQ2022024）
